| Literature DB >> 3753440 |
D H Rich, M A Brown, A J Barrett.
Abstract
Human cathepsin B was purified by affinity chromatography on the semicarbazone of Gly-Phe-glycinal linked to Sepharose 4B, with elution by 2,2'-dipyridyl disulphide at pH 4.0. The product obtained in high yield by the single step from crude starting material was 80-100% active cathepsin B. The possibility that this new form of affinity chromatography may be of general usefulness in the purification of cysteine proteinases is discussed.Entities:
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Year: 1986 PMID: 3753440 PMCID: PMC1146748 DOI: 10.1042/bj2350731
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857